ID A0A1I2DJT7_9RHOB Unreviewed; 561 AA.
AC A0A1I2DJT7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=(2S)-methylsuccinyl-CoA dehydrogenase {ECO:0000313|EMBL:SFE80727.1};
GN ORFNames=SAMN04488523_110185 {ECO:0000313|EMBL:SFE80727.1};
OS Sulfitobacter brevis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=74348 {ECO:0000313|EMBL:SFE80727.1, ECO:0000313|Proteomes:UP000198977};
RN [1] {ECO:0000313|EMBL:SFE80727.1, ECO:0000313|Proteomes:UP000198977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11443 {ECO:0000313|EMBL:SFE80727.1,
RC ECO:0000313|Proteomes:UP000198977};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; FOMW01000010; SFE80727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2DJT7; -.
DR STRING; 74348.SAMN04488523_110185; -.
DR OrthoDB; 9775090at2; -.
DR Proteomes; UP000198977; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF25; ACYL-COA DEHYDROGENASE; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000198977}.
FT DOMAIN 179..290
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 296..396
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 411..560
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 561 AA; 61038 MW; 8FFA412458DE7BB2 CRC64;
MAHDGQDIAM AHPVLLDDLL AVTKDALTPV EAVLDKALAS VRALVTEGDR VSAALIEANQ
TAAHGLAWLA TYAQALRQMQ AWADRLKENG QFGEIEQLLH QIGFGEYLAQ IHGGIQMNQG
EMIRLHDLGL SAEDASGFVT PAVSKLIQSG NTQAARTRLV ELMQEQSANA TVGTTGLDEE
LEMIRDQFRR YATEKVEPYA HDWHLKDELI PMEVINDLAE MGVFGLTIPE EFGGFGLSKA
SMVVVSEELS RGYIGVGSLG TRSEIAAELI LCGGTDEQKA QWLPRIASGE ILPTAVFTEP
NTGSDLGALR TRAVKDGDTY RVTGNKTWIT HAARTHVMTL LARTNPDTTD HRGLSMFLAE
KTPGDDATPF PTPGMTGGEI EVLGYRGMKE YELAFDGFEV KSENLLGGEE GKGFKQLMET
FESARIQTAA RAVGVGQSAL DISMQYAQDR KQFGKALINF PRVSSKLAMM AVELMIARQL
TYFSAWEKDH GRRCDLEAGM AKLLGARVAW AAADNGLQIH GGNGFALEYK ISRVLCDARI
LNIFEGAAEI QAQVIARRLL G
//
